Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis.
To identify potential Sec4 effectors, we isolated high copy suppressors of a Sec4 effector domain mutant. The most potent of these was found to be SEC9, a gene required for post-Golgi transport. The sole essential domain of Sec9 has significant sequence similarity to the neuronal protein SNAP-25, a component of ... the SNARE complex, that is implicated in vesicle targeting and fusion. Analogous to SNAP-25, Sec9 is bound to the yeast plasma membrane and is absent from post-Golgi vesicles. Furthermore, Sec9 is physically associated with two proteins that are homologous to components of the neuronal SNARE complex. Our results identify Sec9 as the yeast cognate of SNAP-25 and suggest that SNARE complexes acting at specific stages of vesicular transport serve as the ultimate targets of regulation by members of the Sec4/Ypt1/Rab family of GTPases.
Mesh Terms:
Amino Acid Sequence, Cell Membrane, Exocytosis, Fungal Proteins, GTP-Binding Proteins, Membrane Proteins, Molecular Sequence Data, Mutagenesis, Site-Directed, Nerve Tissue Proteins, Qa-SNARE Proteins, Qc-SNARE Proteins, R-SNARE Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Structure-Activity Relationship, Synaptosomal-Associated Protein 25, rab GTP-Binding Proteins
Amino Acid Sequence, Cell Membrane, Exocytosis, Fungal Proteins, GTP-Binding Proteins, Membrane Proteins, Molecular Sequence Data, Mutagenesis, Site-Directed, Nerve Tissue Proteins, Qa-SNARE Proteins, Qc-SNARE Proteins, R-SNARE Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Structure-Activity Relationship, Synaptosomal-Associated Protein 25, rab GTP-Binding Proteins
Cell
Date: Oct. 21, 1994
PubMed ID: 7954793
View in: Pubmed Google Scholar
Download Curated Data For This Publication
14961
Switch View:
- Interactions 8